Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock.
about
The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like StructureInvolvement of the twin-arginine translocation system in protein secretion via the type II pathwayIdentification of functional Tat signal sequences in Mycobacterium tuberculosis proteinsBiogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organellesDistinct constrictive processes, separated in time and space, divide caulobacter inner and outer membranes.Structural studies on a twin-arginine signal sequence.Genetic analysis of the twin arginine translocator secretion pathway in bacteria.Localization of the Tat translocon components in Escherichia coli.Effects of the twin-arginine translocase on the structure and antimicrobial susceptibility of Escherichia coli biofilms.Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway.A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.Genetic analysis of G protein-coupled receptor expression in Escherichia coli: inhibitory role of DnaJ on the membrane integration of the human central cannabinoid receptor.Versatile selection technology for intracellular protein-protein interactions mediated by a unique bacterial hitchhiker transport mechanismFeedback inhibition in the PhoQ/PhoP signaling system by a membrane peptideVisualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.Inefficient Tat-dependent export of periplasmic amidases in an Escherichia coli strain with mutations in two DedA family genesSimple genetic selection protocol for isolation of overexpressed genes that enhance accumulation of membrane-integrated human G protein-coupled receptors in Escherichia coliA comprehensive analysis of filamentous phage display vectors for cytoplasmic proteins: an analysis with different fluorescent proteins.Comprehensive engineering of Escherichia coli for enhanced expression of IgG antibodiesCharacterization of fluorescent chimeras of cholera toxin and Escherichia coli heat-labile enterotoxins produced by use of the twin arginine translocation systemRapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysisThe twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases.Protein targeting by the twin-arginine translocation pathway.Multi-copy genes that enhance the yield of mammalian G protein-coupled receptors in Escherichia coli.Vital dye reaction and granule localization in periplasm of Escherichia coliThe flagellar protein FliL is essential for swimming in Rhodobacter sphaeroides.Protein diffusion in the periplasm of E. coli under osmotic stress.Bacterial cell wall synthesis: new insights from localization studiesProduction of secretory and extracellular N-linked glycoproteins in Escherichia coli.The dynamic microbe: green fluorescent protein brings bacteria to light.Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway.Activity of Bdellovibrio hit locus proteins, Bd0108 and Bd0109, links Type IVa pilus extrusion/retraction status to prey-independent growth signalling.Discovery of Salmonella virulence factors translocated via outer membrane vesicles to murine macrophages.Using superfolder green fluorescent protein for periplasmic protein localization studies.The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coliContribution of the twin arginine translocation system to the virulence of enterohemorrhagic Escherichia coli O157:H7Corynebacterium glutamicum possesses β-N-acetylglucosaminidaseTwo electrical potential-dependent steps are required for transport by the Escherichia coli Tat machinery.The Tat pathway in bacteria and chloroplasts (review).Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles.
P2860
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P2860
Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock.
description
2000 nî lūn-bûn
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2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Translocation of jellyfish gre ...... response to osmotic up-shock.
@ast
Translocation of jellyfish gre ...... response to osmotic up-shock.
@en
type
label
Translocation of jellyfish gre ...... response to osmotic up-shock.
@ast
Translocation of jellyfish gre ...... response to osmotic up-shock.
@en
prefLabel
Translocation of jellyfish gre ...... response to osmotic up-shock.
@ast
Translocation of jellyfish gre ...... response to osmotic up-shock.
@en
P2093
P2860
P356
P1476
Translocation of jellyfish gre ...... response to osmotic up-shock.
@en
P2093
Bernadac A
Santini CL
P2860
P304
P356
10.1074/JBC.C000833200
P407
P577
2000-11-30T00:00:00Z